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Characterization and chromosomal localization of USP3, a novel human ubiquitin-specific protease

Sloper-Mould, K; Eyre, Helen; Wang, Xiao Wen; Sutherland, Grant; Baker, Rohan

Description

Conjugation to the small eukaryotic protein ubiquitin can functionally modify or target proteins for degradation by the proteasome. Removal of the ubiquitin modification, or deubiquitination, is performed by ubiquitin- specific proteases and is an important mechanism regulating this pathway. Here we describe a novel human ubiquitin-specific protease, USP3, initially identified as a partial cDNA clone similar to one of two highly conserved sequence regions common to all ubiquitin-specific...[Show more]

dc.contributor.authorSloper-Mould, K
dc.contributor.authorEyre, Helen
dc.contributor.authorWang, Xiao Wen
dc.contributor.authorSutherland, Grant
dc.contributor.authorBaker, Rohan
dc.date.accessioned2015-12-13T23:25:08Z
dc.identifier.issn1431-6730
dc.identifier.urihttp://hdl.handle.net/1885/92530
dc.description.abstractConjugation to the small eukaryotic protein ubiquitin can functionally modify or target proteins for degradation by the proteasome. Removal of the ubiquitin modification, or deubiquitination, is performed by ubiquitin- specific proteases and is an important mechanism regulating this pathway. Here we describe a novel human ubiquitin-specific protease, USP3, initially identified as a partial cDNA clone similar to one of two highly conserved sequence regions common to all ubiquitin-specific proteases. We have isolated a complete USP3 cDNA clone containing both of these conserved sequence regions. The USP3 gene appears to be single copy and maps to human chromosome 15q22.3. A USP3 probe detects two mRNA transcripts, one of which corresponds in length to the cDNA. Both are expressed at low levels in all tissues examined, with highest expression in pancreas. The USP3 protein is a functional ubiquitin-specific protease in vitro, and is able to inhibit ubiquitin-dependent degradation of both an N-end Rule substrate and abnormal endogenous proteins in yeast. USP3 is also only the second known ubiquitin- specific protease capable of efficiently cleaving a ubiquitin-proline bond.
dc.publisherWalter de Gruyter
dc.sourceBiological Chemistry
dc.subjectKeywords: complementary DNA; messenger RNA; proline; proteinase; ubiquitin; ubiquitin specific protease 3; unclassified drug; article; chromosome 15q; conjugation; controlled study; eukaryote; nonhuman; nucleotide sequence; priority journal; protein degradation; pr
dc.titleCharacterization and chromosomal localization of USP3, a novel human ubiquitin-specific protease
dc.typeJournal article
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.citationvolume274
dc.date.issued1999
local.identifier.absfor060107 - Enzymes
local.identifier.ariespublicationMigratedxPub23649
local.type.statusPublished Version
local.contributor.affiliationSloper-Mould, K, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationEyre, Helen, Women's and Children's Hospital
local.contributor.affiliationWang, Xiao Wen, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationSutherland, Grant, Women's and Children's Hospital
local.contributor.affiliationBaker, Rohan, College of Medicine, Biology and Environment, ANU
local.description.embargo2037-12-31
local.bibliographicCitation.issue38
local.bibliographicCitation.startpage26878
local.bibliographicCitation.lastpage26884
local.identifier.doi10.1074/jbc.274.38.26878
dc.date.updated2015-12-12T09:23:39Z
local.identifier.scopusID2-s2.0-0033578890
CollectionsANU Research Publications

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